1Department of Life Sciences, Dibrugarh University, Assam, India.
2Biotechnology Division, Central Muga Eri Research & Training Institute, Central Silk Board, Lahdoigarh, Jorhat, Assam, India.
3Department of Chemistry, Lakhimpur Girls’ College, North Lakhimpur, Assam, India.
Corresponding author email: email@example.com
Article Publishing History
Accepted After Revision:
Naringinase is an omnipotent enzyme found in animals, plants, and microorganisms. Subsequently, naringinase is increasingly getting recognition in industrial application, particularly, in debittering technology of citrus fruit juices. The other industrial sectors considered a potential user of naringinase are antibiotic preparation, wine enhancement, preparation of rhamnose, hydrolysis of glycoside, and biotransformation. Biochemically, naringinase is a multi-complex enzyme, in general, is an enzyme that catalyzes the hydrolysis of α-rhamnose and β-glucose. In addition to this, naringinase can also outnumber other natural glycosides. This natural compound is receiving increasing attention because it carries major potential for application in food and pharmaceutical industries. However, in near future, the growing multifold potential of naringinase application is expected to trigger its share to reach a leading position. The microbial naringinase getting popularity among researchers for its availability, easy handling, multifold property, and abundant supply. In nature, naringinase is obtained from different origins promoting variation in reaction specificity, thus making it a versatile and interesting element of study.
The existence of industrially important microbial strains with diverse genetic resources cannot be ruled out. Isolation and screening of microbial strains found from the diverse ecological niches may lead to the isolation of novel naringinase-producing strains. Research has been conducted worldwide on the isolation of novel naringinase primarily through two different strategies namely; (1) screening of natural resources for isolating microbial strains bearing novel naringinase activity (2) applications of molecular biology tools to develop desired properties from the existing naringinase. The industrial demands of naringinase having high catalytic specificities continue to stimulate the search for new enzyme sources. Hence, an effort has been made through this review to discuss the isolation and characterization of naringinase enzyme along with its applications from different microbial origins in nature.
Bitterness, Debittering, Naringinase, Microorganisms
Pegu B. K, Kardong D, Chutia J, Gogoi D. K, Buragohain M. Microbial Naringinase and its Applications in Debittering Technology –A Mini Review Applications of Microbial Naringinase. Biosc.Biotech.Res.Comm. 2021;14(2).
GPegu B. K, Kardong D, Chutia J, Gogoi D. K, Buragohain M. Microbial Naringinase and its Applications in Debittering Technology –A Mini Review Applications of Microbial Naringinase. Biosc.Biotech.Res.Comm. 2021;14(2). Available from: <a href=”https://bit.ly/3oUsJY0“>https://bit.ly/3oUsJY0</a>
Excessive bitterness is the main problem in the citrus juice industry as it leads to reduced quality and profitable value of the final juice products in the market (Purewal and Sandhu 2021). The processing of citrus fruit juices face forbidding problem of “bitterness” thereby directly affecting consumer acceptability (Lafuente et al. 2021). Without a suitable debittering technology method, the commercial citrus juice industry cannot grow (Narnoliya and Jadaun, 2019; Pangallo et al. 2021). Debittering processed juices looks to be the most favorable method, and some other global citrus juice industries are already furnished with debittering procedures (Curci et al. 2021).
Naringin is a flavanone glycoside, a type of flavonoid. It is glycosylated by a disaccharide at position seven to give a flavanone glycoside. Since naringin and limonin is the principal bitter component of citrus juice, thus, its hydrolysis with a concomitant decreases the bitterness becoming of great industrial importance (Luo et al. 2019). Presently maximum production goes to the fresh fruit market. It is notable that due to poor post-harvest infrastructure, wastage of citrus fruits is around 25-30% and that only a small percentage of the total production is processed due to its problem of bitterness (Sharma et al. 2021).
To control juice quality and improved commercial market value of the citrus juices, namely of grapefruit, maintaining their health properties and increasing consumer acceptance, the reduction of naringin concentration by naringinase hydrolysis is one promising technique having wide industrial application (Gudimella et al. 2021). Limitations of physicochemical technology can be overcomed by introducing the biotechnological methods in fruit juice processing by using naringinase or using whole microbial cells with the ability to produce naringinase as a debittering enzyme, was used in the industrial production of citrus juice (Yu et al. 2021).
Figure 1: Biochemical puri of naringinase enzyme was two steps reaction where naringin a-L- rhamnosidase first split the naringin to prunin (aglycone and D-glucose) liberating on the molecule of L-rhamnose and b-D-glucosidase hydrolysis prunin into non-bitter naringenin liberating one molecule of D glucose (Puri et al. 2010: Rubio 2011; Yadav et al. 2021).
Biochemically, the naringin of certain fruits has sugar complexes (a-L-rhamnose and b-D-glucose) and an aglycone (Naringenin) part. The b-D-glucosidase (EC.184.108.40.206) and a-L- rhamnosidase (EC.220.127.116.11) are collectively known as Naringinase (Beekwilder et al. 2009). The enzyme a-L- rhamnosidase acts on the sugar complex, release prunin, and rhamnose whereas the b-D-glucosidase acts on prunin to release naringenin and glucose (Carqueijeiro et al. 2021).
Naringinase acts on many other natural glucosidases which include hesperidin, diosmin, quercitrin, rutin, naringin, and terphenyl glycosides (Zheng et al. 2021). These substrates have potential chemicals with important properties in the fields of healthcare, food, and agriculture as they are recognized as antioxidant, anti-inflammatory, anti-ulcer, neuroprotective, hypocholesterolemic effects (Torabizadeh et al. 2018; Wang et al. 2021). Microbes are mainly exploited in the industry for naringinase enzyme production. Furthermore, naringinase enzymes are supplied well standardized and market by several competing companies worldwide in recent time (Sheldon et al. 2021). This review focuses on the microbial origin of the naringinase enzyme and its applications.
Microbial Origin of Naringinase Enzymes: A considerable amount of work has been reported from across the globe in the isolation, and purification of naringinase enzymes from different sources of nature. Different microbial sources reported for the naringinase production have been listed in Table 1.
Table 1. In worldwide isolation of different microbial strains production of naringinase enzyme
|Plants||Celery seeds (Apium graveolens)||Hall, (1938)|
|Grapefruit leaves||Ting, (1958)|
|Buckwheat (Fagopyrum esculentum)||Bourbouze et al. (1976)|
|Gastropod||Turbo cornutus||Kurosawa et al. (1973)|
|Mammal||Pig liver||Qian et al. (2005)|
|Fungi||Aspergillus niger||Kishi (1955)|
|Rhamnus dahurica||Suzuki (1962)|
|Aspergillus niger||Bram and Solomons (1965)|
|Cochiobolus miyabeanus and Phanopsis citri||Ito and Takiguchi (1970)|
|Penicillium decumbens||Fukumoto and Okado (1973)|
|Penicillium sp. and||Tsen and Tsai (1988)|
|Penicillium decumbens||Young et al. .,(1989)|
|Penicillium sp.||Hoescht (1994)|
|Penicillium decumbens PTCC 5248||Norouzian et al. .,(1999)|
|Aspergillus niger MTCC 1344||Puri and Karla (2005)|
|Aspergillus niger CECT 2088||Busto et al. .,(2007)|
|Aspergillus niger BCC 25166||Thammawat et al. (2008)|
|Aspergillus niger VB07||Kumar et al. (2010)|
|Aspergillus sojae||Chang et al. (2011)|
|Aspergillus flavus||Radhakrishnan et al. (2013)|
|Aspergillus aculeatus JMUdb058||(Chen et al. 2013)|
|Aspergillus oryzae 1125||Zhu et al. (2017a)|
|Trichoderma longibrachiatum ATCC18648||Housseiny and Aboelmagd (2019)|
|Aspergillus niger van Tieghem MTCC 2425||Borkar et al. (2020)|
|Aspergillus sp. isolate mk156394||Kumar et al. (2020|
|Aspergillus niger KMS||Bodakowska et al. (2020)|
|Aspergillus niger van Tieghem MTCC 2425||Borkar et al. (2020)|
|Penicillium purpurogenum||Patil and Dhake (2020)|
|Aspergillus niger||Gao et al. 2021|
|Aspergillus niger||Gupta et al. (2021)|
|Bacteria||Bacteriodes distasonis, JY-1
|Jang & Kim, (1996)|
|Staphylococcus xylosus MAK2||Puri et al. (2010)|
|Serratia Sp.||Pavithra et al. 2012|
|Micrococcus sp.||Kumar et al.( 2015)|
|Bacillus amyloliquefaciens 11568||Zhu et al. (2017)|
|Bacillus cereus-K1||Pegu et al. (2019)|
|Lactobacillus and Bifi -dobacterium||Tran et al. (2020)|
|Yeast||Williopsis californica Jmudeb007||Ni et al. (2011)|
|Cryptococcus albidusa||Borzova et al. (2017)|
This enzyme has existence in nature and has sources from animal tissues, bacteria, fungi, yeasts, and plants (Yadav et al. 2021). However, for the source of availability, the only process based on microbial naringinase is practicable. There are several reports on the microbial production of naringinase and several production methods from them have been patented, (Puri 2010). Although microorganisms have been reported as the main sources for naringinase enzyme production, these enzymes were first found from a plant source as the first naringinase enzyme was isolated from celery seeds (Hall 1938; Yadav et al. 2021).
Production of Naringinase from Fungal Species: Kishi (1955) first reported fungal naringinase, eventually studied through a 10-L bioreactor to enhance the production of naringinase enzyme by Aspergillus niger (Kishi 1955; Bram and Solomons 1965). Later on, Ito et al. (1970) reported and registered a patent for naringinase production from Cochiobolus miyabeanus Phanopsis citri, and Rhizoctonia solani. For the research by Okada et al. (1973) Penicillium sp. was used for the production of naringinase enzyme (Okada et al. 1973; Yadav et al. 2021).
Naringinase enzyme from Penicillium decumbens has been isolated by (Nourouzian et al. 2000). Whereas, Puri and Karla (2005) purified an extracellular naringinase of Aspergillus niger MTCC 1344 by ion-exchange chromatography. This purified naringinase molecular mass was investigated by SDS-PAGE and found to have 168 kDa. Busto et al. (2007) has reported naringinase production from Aspergillus niger CECT 2008, whereas Thammawat et al. (2008) reported Aspergillus niger BCC 25166 as the most potential naringinase-producing fungi out of 348 fungi isolated from 128 samples, which were collected from 11 different origins in China and Thailand (Thammawat et al. 2008; Yadav et al. 2021).
Later on, Kumar et al. (2010) reported Aspergillus niger VB07 isolates from citrus fruit, producer of extracellular naringinase under various environmental conditions. These authors have studied several inducers used in production for naringinase from Aspergillus niger MTCC-1344 and indicated that naringins are the best inducer for the production of naringinase in a medium. Chang et al. (2011) has isolated Aspergillus sojae from a traditional Korean fermented soybean product. Chen et al. (2013) also reported naringinase enzyme from Aspergillus aculeatus JMUdb058. Later on, Radhakrishnan et al. (2013) isolated Aspergillus flavus and its enzyme naringinase was used for removal of the bitter taste from the juice. Sinthuja et al. (2016) studied the optimization of naringinase production by Rhizophus stolonifer in a solid-state fermentation medium followed by more researches that characterized the enzyme from Aspergillus oryzae (Zhu et al. 2017a; Borkar et al. 2020).
Recently, Borkar et al. (2020) characterized naringinase from Aspergillus niger van Tieghem MTCC 2425. According to Kumar et al. (2020) naringinase has been isolated and studied from Aspergillus sp. isolate mk156394. Similarly, Bodakowska et al. (2020) has reported naringinase enzyme which was immobilized by Aspergillus niger KMS. The production of naringinase by Aspergillus tubingensis MN589840 has also been recently reported that deermines extracellular naringinase production from Aspergillus niger 426 (Xia et al. 2021); Fd et al. 2021). Similarly, Gupta et al. (2021) have characterized naringinase from Aspergillus niger (Gupta et al. 2021).
Bacterial Origins of Naringinase Enzyme : In the previous studies, almost all studies on naringinase targeted fungi as the source, while research on bacterial naringinase was rare. Recently, naringinase produced from bacteria has received more attention, still, only a few naringinase of bacterial origin have been reported (Gupta et al. 2021). Puri et al. (2009) investigated naringinase production from Staphylococcus xylosus MAK2 in a stirred-tank reactor and reported the maximum naringinase production of 8.25 IU/mL at 34th hr. Mukund et al. (2014) discovered new naringinase-producing bacteria Bacillus methylotrophicus commonly found in rhizospheric soil. This study was conducted under optimized culture conditions and obtained the highest naringinase activity of 12 U/L which was 50% more than the activity obtained without optimization. Pavithra et al. (2014) studied the importance of C and N sources for enhancement of naringinase productivity by newly isolate Serratia. Sp (Pavithra et al. 2014; Gupta et al. 2021).
Amena et al. (2015), reported the purification and characterization of naringinase from Micrococcus sp. (Amena et al. 2015). Zhu et al. (2017b) reported the naringinase from a Bacillus amyloliquefaciens 11568 (Zhu et al. 2017b). They have identified, purified, and characterized the enzyme and the purified enzyme molecular weight was found 32 kDa. Tran et al. (2020) carried out a detailed study on four probiotic bacteria strains in which Lactobacillus and Bifidobacterium naringinase gave the maximum production from grapefruit juice fermentation (Tran et al. 2020).
Besides this, only a little literature was found on naringinase production from yeast strains. Ni et al. (2011), reported the naringinase enzyme production from Williopsis californica Jmudeb007 (Ni et al. 2011). Borzova et al. (2017) studied the purification and characterization of naringinase enzyme from Cryptococcus albidusa by Ammonium sulfate fractionation and chromatography. Here, the enzyme had a purified molecular mass of 50kDa. and had an optimum pH at 5.0 as well as temperature of 600C respectively (Borzova et al. 2017; Tran et al. 2020).
Naringinase enzyme is a multi-complex enzyme, in general, is the one that catalyzes the hydrolysis of α-rhamnose and β-glucose. In addition to it, naringinase can also number other glycosides. One unique catalytic property of the naringinase, namely, steroids biotransformation, hydrolysis of glycosidase, renders it to catalyze the reaction in aqueous as well as in the non-aqueous environments. This property of the naringinase ascribes their ability to utilize a wide spectrum of substances, thus increasing the scope of exploiting their specificities in various reactions having importance in pharmaceutical, food, and many other industrial sectors. The industrial demands of naringinase having high catalytic specificities continue to stimulate the search for new enzyme sources. Most of the commercial naringinase are of fungal origins. However, the focus on bacterial and yeast has recently been laid due to their high stability, multifold properties, and abundant supply.
This review paper comprises a literature survey on the work done on naringinase during the last eight decades. Emphasis has been primarily given on the characteristics of naringinase, naringinase production, isolation, and purification. A survey on the recent advances in naringinase technology, such as the preparation of improved varieties of naringinase through molecular biology techniques has also been presented. Further, naringinase may be one of the target enzymes that could be undertaken for isolation from this region. This could be done 1) by screening and use of new more potential naringinase producing microbial strains or 2) by optimizing the culture conditions of selected isolates for commercially viable naringinase production. Therefore, screening of microorganisms with higher naringinase productivity, further the discovery of novel naringinase producing microbial strains is appropriate to new industrial applications.
Authors acknowledge the help and support by Head, Department of Life Sciences, and Dibrugarh University, Assam India.
Conflict of Interests: The authors had no conflict among their interests while researching and preparing this manuscript.
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